6e57: Difference between revisions

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 <StructureSection load='6e57' size='340' side='right'caption='[[6e57]], [[Resolution|resolution]] 2.71&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6e57]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E57 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E57 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6e57]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_ovatus_ATCC_8483 Bacteroides ovatus ATCC 8483]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E57 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E57 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.71&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6e57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e57 OCA], [http://pdbe.org/6e57 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e57 RCSB], [http://www.ebi.ac.uk/pdbsum/6e57 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e57 ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=PRD_900016:beta-cellopentaose'>PRD_900016</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6e57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e57 OCA], [https://pdbe.org/6e57 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e57 RCSB], [https://www.ebi.ac.uk/pdbsum/6e57 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e57 ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/A7LY28_BACO1 A7LY28_BACO1]
-The human gut microbiota, which underpins nutrition and systemic health, is compositionally sensitive to the availability of complex carbohydrates in the diet. The Bacteroidetes comprise a dominant phylum in the human gut microbiota whose members thrive on dietary and endogenous glycans by employing a diversity of highly specific, multi-gene polysaccharide utilization loci (PUL), which encode a variety of carbohydrases, transporters, and sensor/regulators. PULs invariably also encode surface glycan-binding proteins (SGBPs) that play a central role in saccharide capture at the outer membrane. Here, we present combined biophysical, structural, and in vivo characterization of the two SGBPs encoded by the Bacteroides ovatus mixed-linkage beta-glucan utilization locus (MLGUL), thereby elucidating their key roles in the metabolism of this ubiquitous dietary cereal polysaccharide. In particular, molecular insight gained through several crystallographic complexes of SGBP-A and SGBP-B with oligosaccharides reveals that unique shape complementarity of binding platforms underpins specificity for the kinked MLG backbone vis-a-vis linear beta-glucans. Reverse-genetic analysis revealed that both the presence and binding ability of the SusD homolog BoSGBPMLG-A are essential for growth on MLG, whereas the divergent, multi-domain BoSGBPMLG-B is dispensable but may assist in oligosaccharide scavenging from the environment. The synthesis of these data illuminates the critical role SGBPs play in concert with other MLGUL components, reveals new structure-function relationships among SGBPs, and provides fundamental knowledge to inform future (meta)genomic, biochemical, and microbiological analyses of the human gut microbiota.
-Surface glycan-binding proteins are essential for cereal beta-glucan utilization by the human gut symbiont Bacteroides ovatus.,Tamura K, Foley MH, Gardill BR, Dejean G, Schnizlein M, Bahr CME, Louise Creagh A, van Petegem F, Koropatkin NM, Brumer H Cell Mol Life Sci. 2019 May 6. pii: 10.1007/s00018-019-03115-3. doi:, 10.1007/s00018-019-03115-3. PMID:31062073<ref>PMID:31062073</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 6e57" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
+[[Category: Bacteroides ovatus ATCC 8483]]
 [[Category: Large Structures]]
-[[Category: Bahr, C M.E]]
+[[Category: Bahr CME]]
-[[Category: Koropatkin, N M]]
+[[Category: Koropatkin NM]]
-[[Category: Schnizlein, M]]
+[[Category: Schnizlein M]]
-[[Category: Bacteroide]]
-[[Category: Mixed-linkage beta-glucan]]
-[[Category: Sugar binding protein]]
-[[Category: Surface glycan binding protein]]